Characterization of the Geometrical and Electronic Structures of the Active Site and Its Effects on the Surrounding Environment in Reduced High-Potential Iron-Sulfur Proteins Investigated by the Density Functional Theory Approach.

The high-potential iron-sulfur protein (HiPIP) is an electron-transporting protein that functions in the photosynthetic electron-transfer system and possesses a cubane-type [4Fe-4S] cluster in the active center. Characterization of the geometrical and electronic structures of the [4Fe-4S] cluster leads to an understanding of the functions in HiPIP, which are expected to be influenced by the environment surrounding the [4Fe-4S] cluster. This work characterized the geometrical and electronic structures of the [4Fe-4S] cluster in the reduced HiPIP and evaluated their effects on the protein environment using the density functional theory (DFT) approach. DFT calculations showed that the structural asymmetry and spin delocalization between iron atoms allowed for the acquisition of a unique stable geometrical and electronic structure in the open-shell singlet. In addition, the formation of an Fe-Fe bond accompanying the spin delocalization was found to depend on the interatomic distance. A comparison of the calculated stable structures with and without consideration of the amino acids around the [4Fe-4S] cluster demonstrated that the surrounding amino acids stabilized the unique geometrical and electronic structure of the [4Fe-4S] cluster in HiPIP.